1J0C
ACC deaminase mutated to catalytic residue
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-02-01 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0000 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 65.172, 268.265, 186.770 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.750 |
Rwork | 0.224 |
R-free | 0.29850 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 1f2d |
RMSD bond length | 0.007 |
RMSD bond angle | 1.290 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 38.000 * | 2.900 |
High resolution limit [Å] | 2.750 | 2.750 |
Rmerge | 0.073 | 0.353 |
Total number of observations | 241451 * | |
Number of reflections | 43138 | 6182 * |
<I/σ(I)> | 7.9 | 2.5 |
Completeness [%] | 99.9 | 99.6 |
Redundancy | 5.6 | 5.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.5 * | 293 | ammmonium sulfate, pottasium phosphate, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | reservoir | sodium phosphate | 40 (mM) | pH6.5 |
3 | 1 | reservoir | PLP | 100000 (nM) |